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Conserved domains on  [gi|1034638123|ref|XP_016863142|]
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transforming acidic coiled-coil-containing protein 3 isoform X2 [Homo sapiens]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
639-832 1.46e-96

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 299.67  E-value: 1.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 639 YSQKDLDAVVKATQEEN-------RELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQL 711
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 712 TTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQA 791
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034638123 792 EALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLI 832
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
239-458 6.86e-04

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 239 GGVCAP-AAVATSPPGAIPKEAcgGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTN----------H 307
Cdd:PRK07764  579 GGDWQVeAVVGPAPGAAGGEGP--PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPgvaapehhpkH 656
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 308 LVAGRAMTLSPQEEVAAGQMASSSRSGPvklefDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGR 387
Cdd:PRK07764  657 VAVPDASDGGDGWPAKAGGAAPAAPPPA-----PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638123 388 SGAGEDPPMPASRGSYHLDWDKmddpnfiPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGP 458
Cdd:PRK07764  732 SPAADDPVPLPPEPDDPPDPAG-------APAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD 795
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
639-832 1.46e-96

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 299.67  E-value: 1.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 639 YSQKDLDAVVKATQEEN-------RELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQL 711
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 712 TTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQA 791
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034638123 792 EALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLI 832
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
638-838 3.91e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 638 QYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDrfeevvyQAMEEVQKQKELSKaEIQKVLKEKDQLTTDLNS 717
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE-------EKKELEEKVKDLTK-KISSLKEKIEKLESEKKE 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 718 MEKSFSDLFKRFEKQKeviegYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANE---EIAQVRSKaqaeal 794
Cdd:TIGR04523 536 KESKISDLEDELNKDD-----FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQkekEKKDLIKE------ 604
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034638123 795 alqasLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI 838
Cdd:TIGR04523 605 -----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
PTZ00121 PTZ00121
MAEBL; Provisional
648-837 5.85e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  648 VKATQEENR---ELRSRCEELHGKNLELGKimdrfeevvyqAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSD 724
Cdd:PTZ00121  1307 AKKKAEEAKkadEAKKKAEEAKKKADAAKK-----------KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  725 LFKRFEKQKEVIEGYRKNEESLKKCVEDylARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRK-- 802
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKka 1453
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034638123  803 -EQMRIQSLEKTVEQKTKENE-----ELTRICDDLISKMEK 837
Cdd:PTZ00121  1454 eEAKKAEEAKKKAEEAKKADEakkkaEEAKKADEAKKKAEE 1494
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
647-836 6.20e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 46.49  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 647 VVKATQEENRELRSRCEELHGKNLELGKIMDRFEEV----VYQAMEEVQKQKELSKAEIQKVLKEKDQL--TTDLNSMEK 720
Cdd:COG5185   230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQFENTKEKIaeYTKSIDIKK 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 721 SFSDL---FKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEK-----LQLANEEI----AQVRSK 788
Cdd:COG5185   310 ATESLeeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIvgeveLSKSSEELdsfkDTIEST 389
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034638123 789 AQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKME 836
Cdd:COG5185   390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
239-458 6.86e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 239 GGVCAP-AAVATSPPGAIPKEAcgGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTN----------H 307
Cdd:PRK07764  579 GGDWQVeAVVGPAPGAAGGEGP--PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPgvaapehhpkH 656
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 308 LVAGRAMTLSPQEEVAAGQMASSSRSGPvklefDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGR 387
Cdd:PRK07764  657 VAVPDASDGGDGWPAKAGGAAPAAPPPA-----PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638123 388 SGAGEDPPMPASRGSYHLDWDKmddpnfiPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGP 458
Cdd:PRK07764  732 SPAADDPVPLPPEPDDPPDPAG-------APAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD 795
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
687-788 3.58e-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 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  687 MEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIegyrkNEESLKKCVEDYLARItqegQRYQA 766
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATL-----SEAAREKKEKELQKKV----QEFQR 76
                           90       100
                   ....*....|....*....|...
gi 1034638123  767 LKAHAEEKLQLA-NEEIAQVRSK 788
Cdd:smart00935  77 KQQKLQQDLQKRqQEELQKILDK 99
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
639-832 1.46e-96

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 299.67  E-value: 1.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 639 YSQKDLDAVVKATQEEN-------RELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQL 711
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 712 TTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQA 791
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034638123 792 EALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLI 832
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
638-838 3.91e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 638 QYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDrfeevvyQAMEEVQKQKELSKaEIQKVLKEKDQLTTDLNS 717
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE-------EKKELEEKVKDLTK-KISSLKEKIEKLESEKKE 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 718 MEKSFSDLFKRFEKQKeviegYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANE---EIAQVRSKaqaeal 794
Cdd:TIGR04523 536 KESKISDLEDELNKDD-----FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQkekEKKDLIKE------ 604
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034638123 795 alqasLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI 838
Cdd:TIGR04523 605 -----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
633-838 3.87e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 3.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  633 IVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKnlelgkimdrfeevvyqaMEEVQKQKELSKAEIQKVLKEKDQLT 712
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE------------------IEEERKRRDKLTEEYAELKEELEDLR 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  713 TDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKcvedYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAE 792
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKR----ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034638123  793 ALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI 838
Cdd:TIGR02169  447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
688-826 1.49e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 688 EEVQKQKELSK--AEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEV-------IEGYRKNEESLKKCVEDYLARIT 758
Cdd:TIGR04523 357 ENSEKQRELEEkqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLnqqkdeqIKKLQQEKELLEKEIERLKETII 436
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638123 759 QEGQRYQALKAHAEEKlQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTR 826
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVK-ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
641-837 1.76e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  641 QKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVvYQAMEEVQKQKELSKAEIQKVLKEK-------DQLTT 713
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKqilrerlANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  714 DLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAH---AEEKLQLANEEIAQVRSKaq 790
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQ-- 394
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034638123  791 aealalqasLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEK 837
Cdd:TIGR02168  395 ---------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
PTZ00121 PTZ00121
MAEBL; Provisional
648-837 5.85e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  648 VKATQEENR---ELRSRCEELHGKNLELGKimdrfeevvyqAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSD 724
Cdd:PTZ00121  1307 AKKKAEEAKkadEAKKKAEEAKKKADAAKK-----------KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  725 LFKRFEKQKEVIEGYRKNEESLKKCVEDylARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRK-- 802
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKka 1453
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034638123  803 -EQMRIQSLEKTVEQKTKENE-----ELTRICDDLISKMEK 837
Cdd:PTZ00121  1454 eEAKKAEEAKKKAEEAKKADEakkkaEEAKKADEAKKKAEE 1494
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
647-836 6.20e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 46.49  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 647 VVKATQEENRELRSRCEELHGKNLELGKIMDRFEEV----VYQAMEEVQKQKELSKAEIQKVLKEKDQL--TTDLNSMEK 720
Cdd:COG5185   230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQFENTKEKIaeYTKSIDIKK 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 721 SFSDL---FKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEK-----LQLANEEI----AQVRSK 788
Cdd:COG5185   310 ATESLeeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIvgeveLSKSSEELdsfkDTIEST 389
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034638123 789 AQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKME 836
Cdd:COG5185   390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
648-824 7.66e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 648 VKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAME--EVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDL 725
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 726 FK---RFEKQKEVIEGYRKNEESLKKCVEDYlaritqegQRYQALKAHAEE-KLQLANEEIAQVRSKAQAEALALQ---A 798
Cdd:PRK03918  334 EEkeeRLEELKKKLKELEKRLEELEERHELY--------EEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEeieE 405
                         170       180
                  ....*....|....*....|....*.
gi 1034638123 799 SLRKEQMRIQSLEKTVEQKTKENEEL 824
Cdd:PRK03918  406 EISKITARIGELKKEIKELKKAIEEL 431
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
671-838 1.11e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 671 ELGKIMDRFEEVVyQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDL---FKRFEKQKEVIEGYRKNEESLK 747
Cdd:PRK03918  173 EIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 748 KCVEDYLARITQEGQRYQALKAHAEEkLQLANEEIAQVRSKAQAEALALQAsLRKEQMRIQSLEKTVEQKTKENEELTRI 827
Cdd:PRK03918  252 GSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEER 329
                         170
                  ....*....|.
gi 1034638123 828 CDDLISKMEKI 838
Cdd:PRK03918  330 IKELEEKEERL 340
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
658-837 1.31e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 45.50  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 658 LRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKA------EIQKVLKEKDQLTTDLN----SMEKSFSDLFK 727
Cdd:pfam05557  39 LKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkkkyleALNKKLNEKESQLADARevisCLKNELSELRR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 728 RFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAH------AEEKLQLANEEIAQVRSkaqaeALALQASLR 801
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQqsslaeAEQRIKELEFEIQSQEQ-----DSEIVKNSK 193
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034638123 802 KEQMRIQSLEKTVEQKTKENEEL-TRICDDLISKMEK 837
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHLnENIENKLLLKEEV 230
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
653-836 1.41e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.48  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 653 EENRELRSRCEELHGKNLELGKIMDRFEEVVYqameEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEK- 731
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIH----DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKl 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 732 ---QKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANeEIAQVRSKAQAEALALQASLRKEQMRIQ 808
Cdd:pfam05483 498 lleNKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD-ELESVREEFIQKGDEVKCKLDKSEENAR 576
                         170       180
                  ....*....|....*....|....*...
gi 1034638123 809 SLEKTVEQKTKENEELTRICDDLISKME 836
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIE 604
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
645-838 2.64e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  645 DAVVKATQEENRELRSRCEELHGKNLELgkimdrfeevvYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSD 724
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAEL-----------EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  725 LFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEgqryQALKAHAEEKLQLANEEIAQVrSKAQAEALALQASLRKE- 803
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA----EEELAEAEAEIEELEAQIEQL-KEELKALREALDELRAEl 812
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034638123  804 ----------QMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI 838
Cdd:TIGR02168  813 tllneeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
663-838 4.51e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 663 EELHGKNLELGKIMDRFEEVVYQAMEEVQ---KQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDL---FKRFEKQKEVI 736
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEeelKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 737 EGYRKNEEsLKKCVEDYLARITQEGQRYQALKaHAEEKLQLANEEIAQVRSKAQAEALALQASLRKE----QMRIQSLEK 812
Cdd:COG4717   129 PLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQ 206
                         170       180
                  ....*....|....*....|....*.
gi 1034638123 813 TVEQKTKENEELTRICDDLISKMEKI 838
Cdd:COG4717   207 RLAELEEELEEAQEELEELEEELEQL 232
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
656-838 6.12e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 656 RELRSRCEELHG------KNLELGKIMDRFE-EVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKR 728
Cdd:COG1196   196 GELERQLEPLERqaekaeRYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 729 FEKQKEVIEGYRKNEESLKKCvedyLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQ 808
Cdd:COG1196   276 LEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                         170       180       190
                  ....*....|....*....|....*....|
gi 1034638123 809 SLEKTVEQKTKENEELTRICDDLISKMEKI 838
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEEL 381
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
239-458 6.86e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 239 GGVCAP-AAVATSPPGAIPKEAcgGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTN----------H 307
Cdd:PRK07764  579 GGDWQVeAVVGPAPGAAGGEGP--PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPgvaapehhpkH 656
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 308 LVAGRAMTLSPQEEVAAGQMASSSRSGPvklefDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGR 387
Cdd:PRK07764  657 VAVPDASDGGDGWPAKAGGAAPAAPPPA-----PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638123 388 SGAGEDPPMPASRGSYHLDWDKmddpnfiPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGP 458
Cdd:PRK07764  732 SPAADDPVPLPPEPDDPPDPAG-------APAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD 795
PTZ00121 PTZ00121
MAEBL; Provisional
649-838 1.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  649 KATQEENRELRSRCEELHGKNLELGKImdrfEEVVYQAMEEVQKQKELSKAEIQKvlKEKDQLTTDLNSMEKSfSDLFKR 728
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKA----DEAKKKAEEDKKKADELKKAAAAK--KKADEAKKKAEEKKKA-DEAKKK 1439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  729 FEKQKEVIEGYRKNEES-----LKKCVE-----DYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQA 798
Cdd:PTZ00121  1440 AEEAKKADEAKKKAEEAkkaeeAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034638123  799 SLRKEQMRIQSLEKTVEQKTKENEELTRIcdDLISKMEKI 838
Cdd:PTZ00121  1520 EAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEEL 1557
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
261-482 1.36e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 261 GGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSP-QEEVAAGQMASSSRSGPVKLE 339
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPaPEALAAARQASARGPGGAPAP 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 340 FDVSDGATSKRAPPPrrlgeRSGLKPPLRKAA---VRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYhldwdkmdDPNFI 416
Cdd:PRK12323  451 APAPAAAPAAAARPA-----AAGPRPVAAAAAaapARAAPAAAPAPADDDPPPWEELPPEFASPAPA--------QPDAA 517
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638123 417 PFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVV------QLAAETP 482
Cdd:PRK12323  518 PAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMfdgdwpALAARLP 589
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
629-837 1.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 629 STGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVvyqamEEVQKQKELSKAEIQKVLKEK 708
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSKRKLEEKI 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 709 DQLTTDLNSMEKSFSDL---FKRFEKQKEVIEGYRKNEESLKKcVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQV 785
Cdd:PRK03918  262 RELEERIEELKKEIEELeekVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638123 786 RskaqaEALALQASLRKEQMRIQSLEKTVE---QKTKENEEL-TRICDDLISKMEK 837
Cdd:PRK03918  341 E-----ELKKKLKELEKRLEELEERHELYEeakAKKEELERLkKRLTGLTPEKLEK 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
642-831 2.06e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  642 KDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAME-------EVQKQKELSKAEIQKVLKEKDQLTTD 714
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERE 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  715 LNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEE---KLQLANEEIAQVRSKAQA 791
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEK 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1034638123  792 EALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDL 831
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
641-815 2.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 641 QKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQ-KEL------------SKAEIQKVLKE 707
Cdd:PRK03918  541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELepfyneylelkdAEKELEREEKE 620
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 708 KDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRK--NEESLKKCVEDYLaritQEGQRYQALKAHAEEkLQLANEEIAqv 785
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKkySEEEYEELREEYL----ELSRELAGLRAELEE-LEKRREEIK-- 693
                         170       180       190
                  ....*....|....*....|....*....|
gi 1034638123 786 rsKAQAEALALQASLRKEQMRIQSLEKTVE 815
Cdd:PRK03918  694 --KTLEKLKEELEEREKAKKELEKLEKALE 721
PTZ00121 PTZ00121
MAEBL; Provisional
640-837 2.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  640 SQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSME 719
Cdd:PTZ00121  1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  720 KSFSDLfKRFEKQKEV----IEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEK---LQLANEEIAQVRSKAQAE 792
Cdd:PTZ00121  1575 DKNMAL-RKAEEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELK 1653
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034638123  793 ALALQASLRKEQMRIQSLE--KTVEQKTKENEELTRICDDLISKMEK 837
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEEdkKKAEEAKKAEEDEKKAAEALKKEAEE 1700
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
647-838 3.11e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 647 VVKATQEENRELRSRCEELHGKNLELGKIMDRFEEvvyqamEEVQKQKELSKAE------------IQKVLKEK------ 708
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ------EINEKTTEISNTQtqlnqlkdeqnkIKKQLSEKqkeleq 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 709 -----DQLTTDLNSMEKSFSDLFKrfEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALkahaeeklqlaNEEIA 783
Cdd:TIGR04523 279 nnkkiKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-----------NEQIS 345
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638123 784 QVRsKAQAEALALQASLRKE----QMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI 838
Cdd:TIGR04523 346 QLK-KELTNSESENSEKQREleekQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
687-788 3.58e-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 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  687 MEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIegyrkNEESLKKCVEDYLARItqegQRYQA 766
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATL-----SEAAREKKEKELQKKV----QEFQR 76
                           90       100
                   ....*....|....*....|...
gi 1034638123  767 LKAHAEEKLQLA-NEEIAQVRSK 788
Cdd:smart00935  77 KQQKLQQDLQKRqQEELQKILDK 99
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
169-393 5.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 169 VSPGKVSGSPEQAVEEnLSSYSLDRRVTPASEtlEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAva 248
Cdd:PRK07764  588 VGPAPGAAGGEGPPAP-ASSGPPEEAARPAAP--AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA-- 662
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 249 TSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPeSTAPTNHLVAGRAMTLSPQEEVAAGQMA 328
Cdd:PRK07764  663 SDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ-ADDPAAQPPQAAQGASAPSPAADDPVPL 741
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638123 329 sssrsgPVKLEFDVSDGATSKRAPPPRRLGERSglkPPLRKAAVRQQKAPQEVEEDDGRSGAGED 393
Cdd:PRK07764  742 ------PPEPDDPPDPAGAPAQPPPPPAPAPAA---APAAAPPPSPPSEEEEMAEDDAPSMDDED 797
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
642-788 6.13e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 642 KDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKA-----EIQKVLKEKDQLTTDLN 716
Cdd:COG1579    27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYEALQKEIESLKRRIS 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638123 717 SMEKSFSDLFKRFEKQKEVIEGYRKNEESLKkcvedylARITQEGQRYQALKAHAEEKLQLANEEIAQVRSK 788
Cdd:COG1579   107 DLEDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAK 171
PTZ00121 PTZ00121
MAEBL; Provisional
636-834 6.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  636 LLQYSQKDLDAVVKATQEENR---ELRSRCEELHGKNLELGK---IMDRFEEVVYQAMEEVQKQKELSKAEIQKVL---- 705
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKmkaEEAKKAEEAKIKAEELKKaeeEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaae 1665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123  706 --------KEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQL 777
Cdd:PTZ00121  1666 eakkaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638123  778 ANEEIAQVRSKAQAEALALQASLRKEQMRIQSlEKTVEQKTKENEELTRICDDLISK 834
Cdd:PTZ00121  1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK-EAVIEEELDEEDEKRRMEVDKKIK 1801
PRK12704 PRK12704
phosphodiesterase; Provisional
678-820 7.25e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 678 RFEEVVYQAMEEVQKQKELSKAEIQ-KVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEgyrKNEESLKK---CVEDY 753
Cdd:PRK12704   39 EAKRILEEAKKEAEAIKKEALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD---RKLELLEKreeELEKK 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638123 754 LARITQEGQRYQALKAHAEEKLQLANEEIAQVrskaqaealalqASLRKEQMRIQSLEKtVEQKTKE 820
Cdd:PRK12704  116 EKELEQKQQELEKKEEELEELIEEQLQELERI------------SGLTAEEAKEILLEK-VEEEARH 169
Yuri_gagarin pfam15934
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
675-824 7.50e-03

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 38.79  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 675 IMDRFEEvvyqAMEEVQKQKELSKAE---------IQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEES 745
Cdd:pfam15934  36 IMDMFEN----KNEQEQQLKEFTVQNqrlacqidnLHETLKDRDHQIKQLQSMITGYSDISENNRLKEEIHDLKQKNCVQ 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638123 746 LKKCVEDYLARITQEGQRYQALKAHaeEKLQLANEEIAQvrskaqaealalqaSLRKEQMRIQSLEKTVEQKTKENEEL 824
Cdd:pfam15934 112 ARVVRKMGLELKGQEEQRVELCDKY--ESLLGSFEEQCQ--------------ELKRANRRVQSLQTRLSQVEKLQEEL 174
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
685-788 7.90e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 685 QAMEEVQKQKELSKAEIQKVLKEKD--------QLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKneesLKKCVEDYLAR 756
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEELEALKARWEAEKELIEEIQE----LKEELEQRYGK 486
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034638123 757 ITQEGQRYQALKAHAEEKLQLANEE-----IAQVRSK 788
Cdd:COG0542   487 IPELEKELAELEEELAELAPLLREEvteedIAEVVSR 523
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
687-784 8.90e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638123 687 MEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEEslkkcvedylARITQEGQRYQA 766
Cdd:pfam03938   7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKE----------QELQKKEQELQQ 76
                          90
                  ....*....|....*...
gi 1034638123 767 LKAHAEEKLQLANEEIAQ 784
Cdd:pfam03938  77 LQQKAQQELQKKQQELLQ 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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